期刊
EMBO JOURNAL
卷 24, 期 6, 页码 1134-1145出版社
WILEY
DOI: 10.1038/sj.emboj.7600578
关键词
knockout; osmotic shock; PDZ; p38 gamma;; stress-activated protein kinase-4/p38 delta
Activation of the p38 MAP kinase pathways is crucial for the adaptation of mammalian cells to changes in the osmolarity of the environment. Here we identify SAP97/ hDlg, the mammalian homologue of the Drosophila tumour suppressor Dlg, as a physiological substrate for the p38 gamma MAP kinase (SAPK3/p38 gamma) isoform. SAP97/ hDlg is a scaffold protein that forms multiprotein complexes with a variety of proteins and is targeted to the cytoskeleton by its association with the protein guanylate kinase-associated protein ( GKAP). The SAPK3/p38 gamma-catalysed phosphorylation of SAP97/ hDlg triggers its dissociation from GKAP and therefore releases it from the cytoskeleton. This is likely to regulate the integrity of intercellular - junctional complexes, and cell shape and volume in response to osmotic stress.
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